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Related Experiment Videos

High affinity mouse-human chimeric Fab against hepatitis B surface antigen.

Biplab Bose1, Navin Khanna, Subrat K Acharya

  • 1Department of Biochemistry, All India Institute of Medical Sciences, Ansari Nagar, New Delhi, PIN-110029, India. sub_sinha2004@yahoo.co.in.

World Journal of Gastroenterology
|January 27, 2006
PubMed
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Researchers created a mouse-human chimeric antibody fragment targeting hepatitis B surface antigen (HBsAg). This engineered antibody retains high affinity and specificity, paving the way for potential therapeutic applications in Hepatitis B infection treatment.

Area of Science:

  • Immunology
  • Biotechnology
  • Virology

Background:

  • Passive immunotherapy for Hepatitis B infection involves antibodies against hepatitis B surface antigen (HBsAg).
  • A previously developed high-affinity mouse single-chain variable fragment (scFv) against HBsAg showed promise but was unsuitable for human therapy due to potential immunogenicity.
  • Chimerization, combining mouse variable regions with human constant regions, is a strategy to reduce antibody immunogenicity.

Purpose of the Study:

  • To engineer a mouse-human chimeric antibody fragment (Fab) against HBsAg.
  • To assess if the chimerization process preserves the binding affinity and specificity of the original mouse antibody.
  • To establish a foundation for developing a full-length chimeric antibody for therapeutic use in Hepatitis B.

Main Methods:

Related Experiment Videos

  • Cloning of the V(H) and V(L) genes from a mouse anti-HBsAg monoclonal antibody.
  • Fusion of mouse antibody genes with human IgG1 CH1 and human kappa C(L) domains to create chimeric genes.
  • Expression and purification of the chimeric Fab fragment in E. coli using a phagemid vector and phage display system.

Main Results:

  • Successful generation and purification of a mouse-human chimeric Fab fragment against HBsAg.
  • In vitro characterization confirmed that the chimeric Fab retained the high affinity and epitope specificity of the original mouse antibody.
  • Optimization of expression in different E. coli strains was performed to enhance yield.

Conclusions:

  • A mouse-human chimeric Fab fragment targeting HBsAg has been successfully developed.
  • The generated chimeric Fab demonstrates preserved binding characteristics, making it suitable for further development.
  • This chimeric Fab fragment serves as a crucial step towards creating a full-length chimeric antibody for therapeutic applications in Hepatitis B treatment.